The vancomycin class of antibiotics has been described as crystalline, amphoteric, strongly levo-rotatory antibiotics of relatively high molecular weight [Williams et al., Topics in Antibiotic Chemistry, 5, pp 119-158 (1980)]. The vancomycin class of antibiotics also exhibits a reversal of inhibition when synthetic peptides terminating in D-alanyl-D-alanine were introduced to whole cell and cell free preparations [Nieto et al. Biochemical Journal, 26, 139 (1972)]. The known members of this class consist of vancomycin, ristocetin, actinoidin, avoparcin, actaplanin, teichomycin A.sub.2, LL-AM-374, A 477, OA 7653 and A 35512B as well as the individual factor antibiotics thereof. A novel vancomycin class antibiotic, designated AAD 216 complex and its individual factor antibiotics, AAD 216A, AAD 216B and AAD. 216C, are disclosed and claimed in U.S. Pat. No. 4,548,974. Isolation and purification of these vancomycin antibiotics entail standard procedures known in the art. The present invention relates to specific affinity chromatography for facile isolation and purification of the vancomycin class of antibiotics.
Affinity chromatography involves the following general steps: (1) contacting an impure solution of the compound to be isolated with a solid carrier matrix to which an immobilizing ligand, capable of forming a sorption complex with said compound, has been attached; (2) forming the sorption complex; (3) removing the impurities and then (4) dissociating the sorption complex in order to isolate the compound in a purified state. Specifically, murein precursors, UDP-muramyl-pentapeptide has been purified utilizing affinity column chromatography on vancomycin-Sepharose [DePedro et al., FEMS Microbiology Letters, 9, pp 215-217 (1980)].